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Database: UniProt
Entry: A0A1H9W1R3_9BACI
LinkDB: A0A1H9W1R3_9BACI
Original site: A0A1H9W1R3_9BACI 
ID   A0A1H9W1R3_9BACI        Unreviewed;       327 AA.
AC   A0A1H9W1R3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Peptide chain release factor 2 {ECO:0000256|ARBA:ARBA00019192, ECO:0000256|HAMAP-Rule:MF_00094};
DE            Short=RF-2 {ECO:0000256|HAMAP-Rule:MF_00094};
GN   Name=prfB {ECO:0000256|HAMAP-Rule:MF_00094};
GN   ORFNames=SAMN05444126_12635 {ECO:0000313|EMBL:SES27845.1};
OS   Salisediminibacterium haloalkalitolerans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Salisediminibacterium.
OX   NCBI_TaxID=1464123 {ECO:0000313|EMBL:SES27845.1, ECO:0000313|Proteomes:UP000199318};
RN   [1] {ECO:0000313|EMBL:SES27845.1, ECO:0000313|Proteomes:UP000199318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10nlg {ECO:0000313|EMBL:SES27845.1,
RC   ECO:0000313|Proteomes:UP000199318};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Peptide chain release factor 2 directs the termination of
CC       translation in response to the peptide chain termination codons UGA and
CC       UAA. {ECO:0000256|ARBA:ARBA00002613, ECO:0000256|HAMAP-Rule:MF_00094}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF2. {ECO:0000256|HAMAP-Rule:MF_00094}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000256|ARBA:ARBA00010835, ECO:0000256|HAMAP-
CC       Rule:MF_00094}.
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DR   EMBL; FOGV01000026; SES27845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9W1R3; -.
DR   STRING; 1464123.SAMN05444126_12635; -.
DR   Proteomes; UP000199318; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 3.30.70.1660; -; 1.
DR   Gene3D; 1.20.58.410; Release factor; 1.
DR   HAMAP; MF_00094; Rel_fac_2; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004374; PrfB.
DR   NCBIfam; TIGR00020; prfB; 1.
DR   PANTHER; PTHR43116; PEPTIDE CHAIN RELEASE FACTOR 2; 1.
DR   PANTHER; PTHR43116:SF3; RF_PROK_I DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; Release factor; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW   Rule:MF_00094}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199318}.
FT   DOMAIN          205..221
FT                   /note="Prokaryotic-type class I peptide chain release
FT                   factors"
FT                   /evidence="ECO:0000259|PROSITE:PS00745"
FT   COILED          16..76
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          234..273
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         212
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   327 AA;  36989 MW;  45D000D25A55504A CRC64;
     MATPSFWDDQ TEAQKVIGET NALKEMTQTY RKLEEELENL EISFQLVEEE GDEELAAEME
     AQLKTLIKEV NAFELQLLLS GPYDKNNAIL EIHPGAGGTE SQDWASMLLR MYTRFAESMN
     FQVDTLDYLP GDEAGVKSVV LQISGPNAYG YLKAEKGVHR LVRISPFDSS GRRHTSFASC
     EVMPELDDNV EVTINSDDLR IDTFRSSGAG GQHVNTTDSA VRITHLPTNT VVSCQSERSQ
     LKNREKAMKA LRSKLHQLEL QKQQEEADEI RGEQSDIGWG SQIRSYVFHP YNMVKDHRTN
     YEVGNTEAVM DGKLMPFIDA YLRKQIE
//
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